Protein Folding, Misfolding, and Disease: Methods and Protocols

ISBN-13: 9781603272216 / Angielski / Twarda / 2011 / 249 str.

Andrew F. Hill; Roberto Cappai; Kevin Barnham

Opis

Protein misfolding is a key feature of many disorders in humans, given that over twenty proteins are known to misfold and cause disease. In Protein Folding, Misfolding, and Disease: Methods and Protocols, experts in the field present a collection of current methods for studying the analysis of protein folding and misfolding, featuring strategies for expressing and refolding recombinant proteins which can then be utilized in subsequent experiments. This detailed volume also covers methods for analyzing the formation of amyloid, protocols for determining the size and structure of native and misfolded proteins, as well as specific examples of where misfolded proteins can be examined using state-of the-art technologies. Written in the highly successful Methods in Molecular Biology series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.Up to date and authoritative, Protein Folding, Misfolding, and Disease: Methods and Protocols offers researchers the tools necessary to move ahead in this vital field."

Spis treści

1. Strategies for Boosting the Accumulation of Correctly Folded Recombinant Proteins Expressed in Escherichia coli

            Ario de Marco

 

2. An Escherichia coli Cell-Free System for Recombinant Protein Synthesis on a Milligram Scale

            Luke A. Miles, Gabriela A.N. Crespi, Han Sen, Andrew F. Hill, and Michael W. Parker

 

3. Synthesis of Peptide Sequences Derived from Fibril-Forming Proteins

            Denis B. Scanlon and John A. Karas

 

4. Refolding Your Protein with a Little Help from REFOLD

            Jennifer Phan, Nasrin Yamout, Jason Schmidberger, Stephen P. Bottomley, and Ashley M. Buckle

 

5. Circular Dichroism and Its Use in Protein Folding Studies

            David T. Clarke

 

6. Distance Measurements by Continuous Wave EPR Spectroscopy to Monitor Protein Folding

            James A. Cooke and Louise J. Brown

 

7. Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding

            Lisa D. Cabrita, Christopher A. Waudby, Christopher M. Dobson, and John Christodoulou

 

8. Diagnostics for Amyloid Fibril Formation: Where to Begin

            Danny M. Hatters and Michael D. Griffin

 

9. Probing Protein Aggregation with Quartz Crystal Microbalances

            Tuomas P.J. Knowles, Glyn L. Devlin, Christopher M. Dobson, and Mark E. Welland

 

10. Dried and Hydrated X-Ray Scattering Analysis of Amyloid Fibrils

            Sally L. Gras and Adam M. Squires

 

11. Solid-State NMR of Amyloid Membrane Interactions

            John D. Gehman and Frances Separovic

 

12. Sedimentation Velocity Analysis of Amyloid Fibrils

            Chi Le Lan Pham, Yee-Foong Mok, and Geoffrey J. Howlett

 

13. Transmission Electron Microscopy of Amyloid Fibrils

            Sally L. Gras, Lynne J. Waddington, and Kenneth N. Goldie

 

14. Surface Plasmon Resonance Spectroscopy: A New Lead in Studying the Membrane Binding of Amyloidogenic Transthyretin

            Xu Hou, David H. Small, and Marie-Isabel Aguilar

 

15. Elucidating the Role of Metals in Alzheimer’s Disease through the Use of Surface Enhanced Laser Desorption / Ionisation Time-of-Flight Mass Spectrometry

            Andrew D. Watt, Keyla A. Perez, and Lin Wai Hung